Baked goods, such as, cakes, cookies, muffins, bread and rolls, and various baked snacks, are popular foods with many common ingredients. These ingredients may include, for example, but not limited to, one or more of flour, sugar, oil, water, butter, and eggs or an egg protein-based agent. The dough, batter, or other material is typically a combination of two or more of these many ingredients.
Egg and egg protein-based agents in commercially available baked products, such as, for example, cakes and cookies, may serve as an emulsifying agent to help stabilize the oil/water emulsion, in addition to imparting a desirable flavor and/or texture to the product. However, egg-based agents may possess undesirable characteristics, making their inclusion in the formulation problematic. Some of these undesired characteristics include, for example, but not limited to, problems with egg allergies, medical problems associated with cholesterol levels in eggs, religious restrictions/convictions, culinary preferences (such as, for example, a vegetarian or vegan diet), high cost and/or cost fluctuations in the price of eggs, use of antibiotics and hormones during poultry production, and diseases associated with poultry (such as, for example, bird flu). Therefore, in certain baked products it may be desirable to reduce or eliminate the content of egg and/or egg-based protein. However, eggs and egg-based protein agents can impart certain desirable qualities in baked products, for example, taste, strength, stability, and/or firmness. Thus, a substitute for the egg or egg based protein agent that can provide the desired characteristics of eggs while reducing the undesired characteristics would be useful.
In a baked good, emulsifying agents allow insoluble components of the composition, such as the water and the oil, to form a uniform emulsion before heating, and thus produce a uniform final baked good after heating. Emulsifying agents, however, may add height or volume to a baked good thereby weakening the structure of the baked good, and therefore the egg or egg based protein agent may be used to add strength to the baked good because of the added height or volume. Decreasing egg content due to the undesirable properties of eggs may have the unwelcome effects of reducing the strength, stability, and/or firmness of the baked good. This reduction of strength, stability, and firmness may lead to other undesirable qualities, such as reduced volume and increased runniness. In order to reduce the use of egg and egg-based protein agents because of their undesirable qualities, and yet maintain the desirable physical properties of a baked product, the use of alternative proteinaceous emulsifying agents may be desired.
Wheat flour is ideal for making bread and other baked goods since the storage proteins of wheat form a strong, cohesive dough that retains gas bubbles, such as carbon dioxide, produced during rising of bread products to produce light, baked products. The wheat proteins may be isolated from wheat flour by removing starch and albumins/globulins by gently working the dough under a stream of water. After washing, a rubbery ball remains comprising the wheat gluten proteins, which are known as “vital wheat gluten”. Traditionally, gluten proteins have been classified into four families according to their solubility: albumins, which are soluble in water or dilute salt solutions and are coagulated by heat; globulins, which are insoluble in pure water but soluble in dilute aqueous salt solutions and insoluble in concentrated aqueous salt solutions; prolamins, which are soluble in aqueous alcohol; and glutelins, which are soluble in dilute acid or bases, detergents, or dissociating or reducing agents, such as urea or 2-mercaptoethanol, respectively.
The prolamins are considered to be unique to the seed of cereals and other grains or grasses. The prolamins have been given different names in different cereals, such as: gliadin in wheat, avenins in oats, zeins in maize, secalins in rye, and hordein in barley. The gliadins and glutenins of wheat are the storage proteins of the wheat endosperm. Wheat gluten can be described as having a bimodal distribution between gliadin and glutenin. Wheat gluten composition is a major factor in determining wheat dough mixing strength and processing characteristics.
Gliadin, or the gliadin fraction of gluten, has a low ionic strength and excellent film forming properties. Gliadin is insoluble in water; however, its solubility may be modified with the addition of a surfactant and/or adjustment of the pH by acidification. Typical acids suitable for solubilizing gliadin include citric acid, malic acid, lactic acid, oxalic acid, tartaric acid, ascorbic acid, and acetic acid. Gliadin may absorb up to twice its weight of water.
Glutenin, or the glutenin fraction of gluten, is highly elastic and rubbery and is also resistant to shear. Glutenin is insoluble in alcohol and neutral water, however, its solubility may be modified with the addition of a surfactant and/or adjustment of the pH. The protein structure of glutenin is stabilized by interchain disulfide bonds.
Vital wheat gluten is approved by the U.S. Food and Drug Administration as Generally Recognized as Safe (GRAS) under 21 C.F.R. §184.1322 for use as a dough strengthener, formulation aid, nutrient supplement, processing aid, stabilizer and thickener, surface finishing agent, and texturizing agent at levels not to exceed current good manufacturing practice. Vital wheat gluten is defined as a viscoelastic gluten that is extensible when hydrated. As used herein, the term “extensible” includes capable of being stretched without tearing.
Through further removal of non-protein constituents, the protein content of vital wheat gluten can be increased. The functional properties of this protein may also be modified through the use of acids, reducing agents, phosphates, enzymes, and combinations of any thereof to convert the proteins to a “wheat protein isolate”.
Egg replacers and emulsifiers, separately, are known. However, the known egg replacers may not be easy to process or easy to incorporate into food products, nor may they satisfactorily reproduce the texture and flavor associated with baked goods containing eggs or egg based protein agents. Other types of protein may produce a noticeable, undesirable flavor in a baked good when used as a replacement for egg or egg-based protein. In addition, other types of protein may themselves have other undesirable characteristics such as, but not limited to, having allergenic properties. In addition, the prior art egg replacers and emulsifiers may also be liquid, making them difficult to transport and also difficult to scale; and the known compositions may not be configured to replace a substantial percentage of the egg in the baked good. Thus, there is a need for new, easy to use egg replacement and emulsifier systems.